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The Blood Type Diet Archives Volume 3




Re: Dr. D'Adamo: what is the current state of lectin research?

Posted By: researcher
Date: February-19, 1998 at 02:36:47

In Response To: Dr. D'Adamo: what is the current state of lectin research? (David S.)

Here's a couple things to look at. Really, you could just type 'lectins' into a medline search and come up with more than you ever wanted. I summarized a few articles here: if you need more, I have more. Here's free access to medline: just type in lectins or make it a more narrow search if you want.
http:/www.healthy.net/library/search/medline.htm

CANCERS

Bladder Cancer

WGA lectin binds to 6 lines of bladder cancer cells and then when human alveolar macrophages bind, they are more effective in cytotoxicity. Without the WGA they (the AMís) have to be stimulated in other ways before theyíre tumoricidal. (Ogawara et.al. 1987)

WGA induced tumoricidal activity of human blood monocytes which were then cytotoxic to 4 different human tumor cell lines. (T-24 bladder carcinoma, A-375 melanoma, ACHN renal carcinoma and U373MG glioblastoma. (Sharon and Lis 1972)

WGA induced significant and reproducible lectin-dependent macrophage-mediated cytotoxicity against human bladder cancer (T-24) cells. WGA binds to the tumor cell and the Alveolar macrophage, specifically targeting the tumor. Alveolar macrophages and monocytes are affected the same amount by WGA although AMís have more receptors than blood monocytes for WGA. WGA may function in mediating lectin-dependent macrophage mediated cytotoxicity in lung tumors. (Ogawara 1997)

Breast Cancer

ABL lectin from the edible mushroom Agaricus bisporus causes human colorectal and breast carcinoma cells to stop proliferating (dose dependent). No toxic effects. (Lugang et.al. 1993)

PNA binding to breast cancer cells inhibited proliferation in culture. Not all breast cancer cell lines can bind PNA. Retinoic acid, which reduces PNA binding, did not reduce PNAís effect on proliferation. The combination lead to an additive growth-inhibitory action. In one case PNA binding made a cell line more susceptible to interferon y. (Marth and Daxinbichler 1988)

HPA binds breast cancer tissue when it is near metastatic stage. Since it is an agglutinin it probably causes these cells to clump up an maybe be more easily targeted by the immune system. (Fenlon 1987)**Does HPA have a higher preference for cancerous cells than normal human cells, because it is a type A agglutinin, and if it doesnít then it would be harmful for type Aís.

HPA binds to Breast cancer cells. (Brooks and Leathem 1991)

ABL lectin can bind sialyated Gal-1,3-Nacetylgalactosamine. ABL inhibits incorporation of [3H]thymidine into DNA of HT-29 colon cancer cells by 87%m /caca-2 Colon cancer cells by 16%, MCF-7 breast cancer cells by 50% and Rama-27 rat mammary fibroblasts by 55% (Yu et.al. 1993)

In human breast cancer (MDA-MB-435 cell line) synthetic glycosamines blocked PNA lectins interaction with B-gal. Synthetics used were Fru-D-Leu and Lac-L-Leu.. Fru-L-Leu had anti-metastatic action in vitro but not in vivo. (Glinsky et.al. 1996)

Peanut agglutinin strongly binds to normal mammary epithelium and this binding strength is progressively lost with increasing malignancy (50 times less strong when malignant) (Rak et.al. 1992)

ML-1 is galactose specific, ML-2 is Galactose and N-acetyl-D-galactosamine specific and ML-3 is N-acetyl galactosamine specific. Several studies have shown that immunological parameters of cancer patients can be changed favorably by the application of mistletoe extracts containing MLís. The dose of ML-1required to be toxic to breast cancer cells (10 ng/ml) is 40X higher than he dose needed to activate lymphocytes in culture. Immunostimulatory effects could be observed after giving patients suffering from advanced breast cancer 1 ng of ML-1 per kg body weight for 4 weeks. ML-1 and 3 have almost identical binding characteristics, and ML-2 is different. (Schumacher et.al. 1995)

HPA binding to breast cancer material is probably linked to the presence of nodal metastases rather than proliferative rate or ploidy. (Brooks et.al 1993)

In metastatic breast cancer there are a number of cell membrane constituents known to contain N-acetylgalactosamine residues that may be of structural importance like epidermal growth factor and the transferrin receptor. EGF expression increases in bad prognosis breast cancers and may act as a cell-adhesion molecule, therefore it may be important in metastasis. Iron is essential for metabolism of breast cancer cells. (Mitchell et.al.1995)

Expression of PNA receptor binding sites in ductal breast cancer cells is associated with the expression of estrogen receptors in these cells. It measures the functional differentiation of tumor cells via differential expression of glycoproteins. (Mustak et.al. 1996)

Colorectal Cancer

ABL lectin from the edible mushroom Agaricus bisporus causes human colorectal and breast carcinoma cells to stop proliferating (dose dependent). No toxic effects. (Lugang et.al. 1993)

ABL lectin can bind sialyated Gal-1,3-Nacetylgalactosamine. ABL inhibits incorporation of [3H]thymidine into DNA of HT-29 colon cancer cells by 87%m /caca-2 Colon cancer cells by 16%, MCF-7 breast cancer cells by 50% and Rama-27 rat mammary fibroblasts by 55% (Yu et.al. 1993)

One of the most commonly exhibited abnormalities in malignant and hyperplastic epithelia is increased expression of the blood group TF antigen (structure : galactosyl B-1,3-N-acetylgalactosamine alpha). This structure is recognized by PNA which acts as a mitogen and is resistant to digestion. Therefore Gal-beta-1,3-N-acetylgalactosamine binding dietary lectins could act as tumor promoters in the colon. (Yu et.al 1993)

Galectin-3 is expressed more with increasing dysplasia in advancing stage colon cancer compared to tissues the dysplasia originated from. Galectin-3 is also known as Mac-2, CBP-35, IgEBP, CBP-30, RL-29, hL-31, mL-34 and LBL. This is especially true for lymph nodes and liver metastases. (Schoeppner et.al. 1995)

HPA binds to breast cancers with a poor prognosis. Also prognostic for stomach, prostate and colon carcinomas. But the HPA binding glycoconjugates have not yet been identified nor have any cellular functions related to the metastatic cascade been attributed to identified HPA-binding glycoconjugates. No over-expression of any particular HPA glycoprotein is obvious in breast cancer cells. HPA can bind several glycoproteins. (Schumacher et.al. 1995)

Glioblastoma

WGA induced tumoricidal activity of human blood monocytes which were then cytotoxic to 4 different human tumor cell lines. (T-24 bladder carcinoma, A-375 melanoma, ACHN renal carcinoma and U373MG glioblastoma. (Sharon and Lis 1972)

Leukemia

ML-1 (VAA) has the ability to non-specifically increase immune system defense in the host. It has a dramatic anti-tumor effect, including activating Natural killer cells (NK), enhancing monocyte and macrophage activity, stimulating secretion of cytokines (TNF-alpha and IL-6) without any toxic effects. It induces apoptosis in human myelomonocytic leukemic cells. (Mody et.al. 1995)

Neutrophils create superoxide dismutase which plays a large part in tumor defense. Neutrophils of lung cancer patients or patients with chronic neutrophilic leukemia can not make as much SOD in response to Phorbol 12-myristate 13acetate. If you can increase their ability to produce superoxide, this may benefit the hostís defense system. This activity can be stimulated by Concavalin A (mannose specific), WGA (N-acetylglucosamine, neuraminic acid specific), Viscum album lectins (galactoside-specific) and human placenta. The lectins bind with different affinities because they bind different moieties. Con A had a stronger affect than WGA. Standard chemotherapy reduced the ability of neutrophils to produce superoxide when later stimulated by Con A and reduced also the affect of VAA. Tumor type may affect the responsiveness of the neutrophils- eg. Bronchial carcinoma patients expressed less superoxide when exposed to ConA, mammary carcinoma patients did not. (Timoshenko et.al.1993)

Lung Cancer

PA-1 binds galactose and PA-2 binds L-fucose, D-mannose, L-galactose and D-fructose. All have been used as cytotoxins against Lewis lung cancer cells. (Mody et.al.1995)

WGA induced significant and reproducible lectin-dependent macrophage-mediated cytotoxicity against human bladder cancer (T-24) cells. WGA binds to the tumor cell and the Alveolar macrophage, specifically targeting the tumor. Alveolar macrophages and monocytes are affected the same amount by WGA although AMís have more receptors than blood monocytes for WGA. WGA may function in mediating lectin-dependent macrophage mediated cytotoxicity in lung tumors. (Ogawara 1997)

Neutrophils create superoxide dismutase which plays a large part in tumor defense. Neutrophils of lung cancer patients or patients with chronic neutrophilic leukemia can not make as much SOD in response to Phorbol 12-myristate 13acetate. If you can increase their ability to produce superoxide, this may benefit the hostís defense system. This activity can be stimulated by Concavalin A (mannose specific), WGA (N-acetylglucosamine, neuraminic acid specific), Viscum album lectins (galactoside-specific) and human placenta. The lectins bind with different affinities because they bind different moieties. Con A had a stronger affect than WGA. Standard chemotherapy reduced the ability of neutrophils to produce superoxide when later stimulated by Con A and reduced also the affect of VAA. Tumor type may affect the responsiveness of the neutrophils- eg. Bronchial carcinoma patients expressed less superoxide when exposed to ConA, mammary carcinoma patients did not. (Timoshenko et.al.1993)

Melanoma

WGA induced tumoricidal activity of human blood monocytes which were then cytotoxic to 4 different human tumor cell lines. (T-24 bladder carcinoma, A-375 melanoma, ACHN renal carcinoma and U373MG glioblastoma. (Sharon and Lis 1972)

Synthetic glycoamine can inhibit homotypic aggregation of murine B16 melanoma cell by interfering with B-gal specific lectin-mediated cell-to-cell interactions. Blockage of these galectin-mediated interactions resulted in apoptosis in highly metastatic b16-F10 murine melanoma cell variants. Synthetics used were Fru-D-Leu and Lac-l-Leu. Inhibit cell aggregation and adhesion. Doesnít work well in vivo. (Glinsky et.al. 1996) **Does it not work well in vivo because they didnít use oligosaccharides attached to amino acids?**

Synthetic analog Fru-D-Leu specifically inhibits the binding of both B-D-Gal and T-antigen specific carbohydrate biotinylated probes to the B16-F10 murine metastatic melanoma cells. Itís binding might disrupt carbohydrate recognition and binding. (Glinsky et.al 1996)

Prostate cancer

In high grade intraepithelial neoplasia (PIN) a precursor for peripheral prostatic adenocarcinoma: SBA and Ulex europus agglutinin stained positively in dysplastic glands and carcinoma, not in normal tissues. (Drachenburg et.al. 1995)

HPA binds to breast cancers with a poor prognosis. Also prognostic for stomach, prostate and colon carcinomas. But the HPA binding glycoconjugates have not yet been identified nor have any cellular functions related to the metastatic cascade been attributed to identified HPA-binding glycoconjugates. No over-expression of any particular HPA glycoprotein is obvious in breast cancer cells. HPA can bind several glycoproteins. (Schumacher et.al. 1995)

Renal carcinoma

WGA induced tumoricidal activity of human blood monocytes which were then cytotoxic to 4 different human tumor cell lines. (T-24 bladder carcinoma, A-375 melanoma, ACHN renal carcinoma and U373MG glioblastoma. (Sharon and Lis 1972)

Sarcoma

Red kidney bean lectin agglutinates sarcoma 180 cells (Sharon and Lis 1972)

Stomach cancer

HPA binds to breast cancers with a poor prognosis. Also prognostic for stomach, prostate and colon carcinomas. But the HPA binding glycoconjugates have not yet been identified nor have any cellular functions related to the metastatic cascade been attributed to identified HPA-binding glycoconjugates. No over-expression of any particular HPA glycoprotein is obvious in breast cancer cells. HPA can bind several glycoproteins. (Schumacher et.al. 1995)

LECTINS:

ABRIN

Abrin (from A.precatorius seed) inhibits protein synthesis similarly to ricin. (Leiner 1976)

AGARICUS BISPORUS

ABL lectin from the edible mushroom Agaricus bisporus causes human colorectal and breast carcinoma cells to stop proliferating (dose dependent). No toxic effects. (Lugang et.al. 1993)

ABL lectin can bind sialyated Gal-1,3-Nacetylgalactosamine. ABL inhibits incorporation of [3H]thymidine into DNA of HT-29 colon cancer cells by 87%m /caca-2 Colon cancer cells by 16%, MCF-7 breast cancer cells by 50% and Rama-27 rat mammary fibroblasts by 55% (Yu et.al. 1993)

Red blood cell agglutination by ABL is better inhibited by Gal-N-acetylgalactosamine bearing glyco-proteins than by single sugars. (Yu et.al 1993)

ABL stimulates vascular smooth muscle and endothelial cell proliferation. More potent than PHA, WGA and Vicia Faba, and has no toxicity. (Yu et.al. 1993)

ABL reacts with the TF antigen and inhibits cell proliferation. (Yu et.al. 1993)

ANGUILLA ANGUILLA

A type O specific agglutinin comes from the serum of the eel (Anguilla anguilla). (Sharon and Lis 1972)

CONCAVALIN A

A potent mitogen of human leukocytes. (Mody et.al.1995)

Con-A causes superoxide release from neutrophils- decreasing free oxygen radicals in cancer patients. (Timoshenko et.al 1993)

Con-A lectin from the Jack bean (Canavalia ensiformis) reacts with glycogen. (Sharon and Lis 1972)

Con A is specific to alpha-D-mannopyranosides, alpha-D-glucopyranosides and alpha-N-acetyl-D-glucoaminides. (Sharon and Lis 1972)

Cells transformed by viruses or carcinogens can be agglutinated by Con A more readily than it will agglutinate normal cells, but it can also be mitogenic and cytolitic to some lymph node cells, interacting with fibroblasts. (Sharon and Lis 1972)

Con A agglutinates Leukemic cells and cells that have been transformed by the polyoma virus, simian virus 40, chemical carcinogens and x-ray radiation at a concentration of 250 micrograms /ml which is a lower concentration than will agglutinate normal cells. Agglutination is reversed by methyl alpha-D-glucopyranosides. Removal of bivalent ions from con A abolishes its cell-agglutinating activity. (Sharon and Lis 1972)

Agglutination by ConA might be a 2-step process: 1)a simple mono or divalent binding process which is enough to trigger mitogenesis or to inhibit cell growth and 2)Multivalent process- cross-linking of macromolecules or cell receptor sites causes precipitation of macromolecules or agglutination of the cells respectively. Con A interacts with alpha-D-mannopyranosyl, alpha-D-glucopyranosyl and alpha-D-N-acetyl glucosamine at terminal ends and mannose residues in the interior of the molecule. (Leiner 1976)

Pea lectins (Pisium sativum) activity requires Calcium and magnesium. They have affinity for mannose and glucose. Agglutinates erythrocytes and tumor cells more readily than ConA. (Leiner 1976)

Con A prevents Ehrlich ascites tumor cells from maintaining a normal potassium content, they donít damage the cells through agglutination. Both ricin and con A caused net K loss by stimulating K efflux. Ricin at 2 micrograms /ml is as effective as Con A at 100 micrograms/ml. (Aull et al 1976)

Neutrophils create superoxide dismutase which plays a large part in tumor defense. Neutrophils of lung cancer patients or patients with chronic neutrophilic leukemia can not make as much SOD in response to Phorbol 12-myristate 13acetate. If you can increase their ability to produce superoxide, this may benefit the hostís defense system. This activity can be stimulated by Concavalin A (mannose specific), WGA (N-acetylglucosamine, neuraminic acid specific), Viscum album lectins (galactoside-specific) and human placenta. The lectins bind with different affinities because they bind different moieties. Con A had a stronger affect than WGA. Standard chemotherapy reduced the ability of neutrophils to produce superoxide when later stimulated by Con A and reduced also the affect of VAA. Tumor type may affect the responsiveness of the neutrophils- eg. Bronchial carcinoma patients expressed less superoxide when exposed to ConA, mammary carcinoma patients did not. (Timoshenko et.al.1993)

DOLICHOS BIFLORUS

Agglutinin of type A blood cells. (Sharon and Lis 1972)

Horsegram lectins (D. biflorus) has type A specificity. Eluted with N-acetylgalactosamine. (Leiner 1976)

D.biflorus lectin is non-toxic but orally administered it inhibited the growth of rats. (Liener 1974)

E.COLI

Polysaccharide from E.Coli O86 was very active for blood group B agglutination. (Springer 1958)

HELIX POMATIA

Helix pomatia agglutinates type A blood cells. (Sharon and Lis 1972)

HPA binds breast cancer tissue when it is near metastatic stage. Since it is an agglutinin it probably causes these cells to clump up an maybe be more easily targeted by the immune system. (Fenlon 1987)**Does HPA have a higher preference for cancerous cells than normal human cells, because it is a type A agglutinin, and if it doesnít then it would be harmful for type Aís.

HPA positive tumors in young people seem to be more aggressive but in older people (post-menopausal) they are not overly aggressive. (Leathem 1987)

HPA binds to Breast cancer cells. (Brooks and Leathem 1991)

HPA binds to breast cancers with a poor prognosis. Also prognostic for stomach, prostate and colon carcinomas. But the HPA binding glycoconjugates have not yet been identified nor have any cellular functions related to the metastatic cascade been attributed to identified HPA-binding glycoconjugates. No over-expression of any particular HPA glycoprotein is obvious in breast cancer cells. HPA can bind several glycoproteins. (Schumacher et.al. 1995)

Positive rate of HPA binding was related to the gene amplification of c-myc, a proto-oncogene (p<0.01). (Fukutomi et.al. 1991) **Is the c-myc product a glycoprotein???**

.3M N-acetylgalactosamine was able to completely inhibit the agglutination of type A red blood cells. This didnít completely inhibit the binding of HPA, though, so itís probably got a slightly more complex binding site than just the A antigen. (Schumacher et.al 1992)

HPA binds to breast cancers, gastric cancer, colorectal cancer and prostate cancer when theyíre at a distant metastasis stage with poor prognosis. HPA recognizes alpha-linked terminal N-acetylgalactosamine in (e.g.) the Tn antigen. The actual binding site includes subterminal sugars also and the arrangement of the molecules in space must also be right. A lot of glycoproteins bound (determined by SDS PAGE) breast cancer tissues but one bound specifically to breast cancer and NOT normal tissues, determined to be the IGA-1 heavy chain. (Streets et.al 1996)

HUMAN PLACENTA LECTIN

Human placenta lectin causes superoxide release from neutrophils, decreasing free oxygen radicals in cancer patients. (Timoshenko et.al. 1993)

Neutrophils create superoxide dismutase which plays a large part in tumor defense. Neutrophils of lung cancer patients or patients with chronic neutrophilic leukemia can not make as much SOD in response to Phorbol 12-myristate 13acetate. If you can increase their ability to produce superoxide, this may benefit the hostís defense system. This activity can be stimulated by Concavalin A (mannose specific), WGA (N-acetylglucosamine, neuraminic acid specific), Viscum album lectins (galactoside-specific) and human placenta. The lectins bind with different affinities because they bind different moieties. Con A had a stronger affect than WGA. Standard chemotherapy reduced the ability of neutrophils to produce superoxide when later stimulated by Con A and reduced also the affect of VAA. Tumor type may affect the responsiveness of the neutrophils- eg. Bronchial carcinoma patients expressed less superoxide when exposed to ConA, mammary carcinoma patients did not. (Timoshenko et.al.1993)

LENS ESCULENTA

Subspeices microsperma. Most lentil lectins show no specificity toward ABO human erythrocytes but L.esculenta has blood group A specificity. (Leiner 1976)

LOTUS TETRAGONOLOBUS

Crude extract from Lotus was more effective as a type O agglutinin than as a purified extract. (Sharon and Lis 1972)

Lotus tetragonolobus (asparagus pea) exhibits specificity for the H-determinant of O-group human erythrocytes and is inhibited by L-fucose. (Leiner 1976)

MACLURA POMIFERA AGGLUTININ

A potent mitogen of human leukocytes. (Mody et.al. 1995)

Osage orange (Maclura pomifera) is inhibited with D-galactose sugars. (Leiner 1976)

MISTLETOE LECTINS

7 different types of mistletoe extracts are commercially available with variable anticancer effects- especially ML-1. (Mody et.al. 1995)

ML-1 (VAA) has the ability to non-specifically increase immune system defense in the host. It has a dramatic anti-tumor effect, including activating Natural killer cells (NK), enhancing monocyte and macrophage activity, stimulating secretion of cytokines (TNF-alpha and IL-6) without any toxic effects. It induces apoptosis in human myelomonocytic leukemic cells. (Mody et.al. 1995)

ML-1 increased B-endorphin plasma levels, increased blood lymphatic subsets after chemotherapy and caused release of cytokines. It is immunoactive and a painkiller. Dramatic antimetastatic effects with subcutaneous administration of 1 ng/kg of body weight two times per week in murine systems. (Heiny and Beuth 1994)

1 ng/kg body weight of ML-1 (galactoside specific) per day for 12 weeks caused 1) significant increase in B-endorphin plasma levels and 2) An increase in defined peripheral blood lymphatic subsets after standard chemotherapy 3)Increased in vitro cytokine release by mononuclear immune cells after stimulation. (Heiny and Beuth 1994)

ML-1 is galactose specific, ML-2 is Galactose and N-acetyl-D-galactosamine specific and ML-3 is N-acetyl galactosamine specific. Several studies have shown that immunological parameters of cancer patients can be changed favorably by the application of mistletoe extracts containing MLís. The dose of ML-1required to be toxic to breast cancer cells (10 ng/ml) is 40X higher than he dose needed to activate lymphocytes in culture. Immunostimulatory effects could be observed after giving patients suffering from advanced breast cancer 1 ng of ML-1 per kg body weight for 4 weeks. ML-1 and 3 have almost identical binding characteristics, and ML-2 is different. (Schumacher et.al. 1995)

VAA can modulate other cell functions in the immune system like cytokine secretion and NK cell activity, applying it along with other treatments may or nay not be beneficial for the patient depending on the personís extent of reactivity. (Timoshenko et.al 1993)

PEANUT AGGLUTININ

PNA binding to breast cancer cells inhibited proliferation in culture. Not all breast cancer cell lines can bind PNA. Retinoic acid, which reduces PNA binding, did not reduce PNAís effect on proliferation. The combination lead to an additive growth-inhibitory action. In one case PNA binding made a cell line more susceptible to interferon y. (Marth and Daxinbichler 1988)

PNA binds Gal-B-1,3-N-acetylgalactosamine and stimulates proliferation in HT-29 human colon cancer cells. (Yu et al. 1993)

One of the most commonly exhibited abnormalities in malignant and hyperplastic epithelia is increased expression of the blood group TF antigen (structure : galactosyl B-1,3-N-acetylgalactosamine alpha). This structure is recognized by PNA which acts as a mitogen and is resistant to digestion. Therefore Gal-beta-1,3-N-acetylgalactosamine binding dietary lectins could act as tumor promoters in the colon. (Yu et.al 1993)

In human breast cancer (MDA-MB-435 cell line) synthetic glycosamines blocked PNA lectins interaction with B-gal. Synthetics used were Fru-D-Leu and Lac-L-Leu.. Fru-L-Leu had anti-metastatic action in vitro but not in vivo. (Glinsky et.al. 1996)

Peanut agglutinin strongly binds to normal mammary epithelium and this binding strength is progressively lost with increasing malignancy (50 times less strong when malignant) (Rak et.al. 1992)

PNA has high affinity for the disaccharide galactose-N-acetylgalactosamine which is also the T-antigen. It reportedly disappears in high grade tumors. WGA may be better correlated than PNA with poor prognosis. (Langkilde et.al. 1989)

PNA binds breast cancer cells, and is associated with presence of estrogen receptors. Asialofetuin administered at a concentration able to displace 70% of the PNA abolished growth-inhibitory action. Although Retinoic acid normally inhibits PNA binding, their combined effect enhanced inhibition of proliferation. Combination with an anti-estrogen was also additive. Interferon Y and PNA were also synergistic in cell line ZR-75-1. Showed increased susceptibility to IF-y when treated with PNA, not necessarily because PNA was bound. (Marth and Daxenbichler 1988)

Very common alteration in malignant tissues is to start to produce the PNA autoantigen. Widespread PNA reactive autoantigen may play a role in tumor escape from the immune system and hence tumor progression. (Laderoute et.al.1994)

Expression of PNA receptor binding sites in ductal breast cancer cells is associated with the expression of estrogen receptors in these cells. It measures the functional differentiation of tumor cells via differential expression of glycoproteins. (Mustak et.al. 1996)

PHASEOLUS COCCINEUS

P. coccineus contains 2 lectins which both agglutinate all blood groups but one is mitogenic for lymphocytes. Inhibited by N-acetylgalactosamine.

PHASEOLUS LIMENSIS

Crude extracts from the lima bean (Phaseolus limensis) are virtually specific for agglutination of the A antigen but when concentrated they can react with type B as well. (Sharon and Lis 1972)


PHASEOLUS LUNATUS

Specific agglutinator of blood type A (Leiner 1976)

Ingestion of P.lunatus (lima bean) agglutinin inhibited the growth of rats. (Liener 1974)

PHASEOLUS VULGARIS

A potent mitogen of human leukocytes. (Mody et.al.1995)

PHA lectin can 1)Help induce remission in many malignancies 2) directly kill tumor cells 3)Reduce neoplasia after chemo and radiotherapy 4) Make metastasis less likely- prevent it 5)Help reverse neoplastic cell condition back to normal responses 6)Build immunity to infection 7)Make tumors more recognizable to the immune system 8)cause cells to produce cytokines 9)Make cells more targetable. (Mody et.al 1995)

P.vulgaris has haemagglutinating, mitogenic and leukoagglutinating activity reacting non-specifically with human blood groups. (Leiner 1976)

Lectins from raw P.vulgaris when fed raw depressed growth of and were toxic to rats and quail. (Liener 1976)

Phaseolus vulgaris (black and kidney beans are both called P.vulgaris) were improved by heat treatment. (Liener 1974)





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